Host defense peptides (HDPs) are a large group of small, positively charged peptides that play an important role in innate immunity, particularly at early ages when other components of the immune system have not fully developed. There are 3 classes of avian HDPs: avian beta defensins (AvBDs), cathelicidins (Cath), and liver-expressed antimicrobial peptide 2 (LEAP-2). The objective was to compare expression of HDP mRNAs in male turkey poults at day of hatch (d 0), d 7, d 14, d 21 and d 28 from the thymus, spleen, bursa, duodenum, jejunum, and ileum. The expression of AvBD1, AvBD2, AvBD8, AvBD9, AvBD10, AvBD13, Cath2, Cath3, and LEAP-2 mRNA was measured using qPCR (n = 6 birds/tissue/age). Data were analyzed by one-way ANOVA and Tukey's test, and significance considered at P < 0.05. AvBDs and Caths exhibited greater expression in immune organs (thymus, spleen, and bursa) than intestinal tissues. In the thymus, expression of all AvBDs examined, except AvBD8, showed an increase from d 0 to d 21. In the spleen, AvBD1 and AvBD2 exhibited reduced expression from d 0 to d 7 and low expression thereafter. In the intestine, AVBD1, AVBD8, and AvBD13 increased expression from d 0 to d 28 in the duodenum, while AvBD10 showed the greatest expression at d 0 that declined to d 7 and stayed low thereafter in the duodenum, jejunum, and ileum. Cath2 and Cath3 demonstrated the highest expression in the spleen, which was greatest at d 0 then declined to d 7 through d 28. Conversely, LEAP-2 showed greater expression in the intestinal tissues than in the immune organs. LEAP-2 expression was upregulated from d 0 to d 7 and then remained elevated from d 7 through d 14 in the duodenum. In the jejunum, LEAP-2 increased from d 0 to d 21 and d 28. Understanding the differential expression of HDPs could reveal the innate immune status of turkey poults, and may subsequently allow improvement of their health through appropriate mitigation strategies.
Sperm cryopreservation is of great importance for the poultry industry but still needs to be optimized. The high susceptibility of poultry sperm to cryodamage leads to low fertility rates after cryopreservation. Therefore, the present study aimed at evaluating the effect of including a cryoprotectant, dimethylacetamide (DMA), in the chicken semen freezing extenders at a final concentration of 3%, 6%, or 9% on the post-thawed sperm motility, quality, antioxidant biomarkers, anti-freeze gene expression, and fertilizing ability. Results showed that the total motile sperm, progressivity, and viability were quadratically increased (p < 0.05) in the 6% DMA group. The antioxidant enzyme activity and lipid peroxidation were negatively (p < 0.05) affected by the increase in DMA concentration. Furthermore, some anti-freeze-associated genes such as heat shock protein 70 (HSP70) and ras homolog family member A (RHOA) were linearly and quadratically down-regulated (p < 0.05) with the high concentration of DMA. Finally, the fertility and hatchability rates did not indicate statistical differences between DMA groups. It can be concluded that using the low concentration of 3–6% DMA in the freezing semen extender is preferable to obtain acceptable results in the post-thawed sperm quality and fertility.
Sperm cryopreservation is an effective technique for conserving animal genetic diversity and transmitting superior genetic backgrounds, maintained via a non-invasive sampling and collection of huge quantities of sperm. Nevertheless, cryopreservation in avian species is not commercially viable because of the rooster sperm’s susceptibility to damage. This study aims to estimate the impact of dimethylacetamide (DMA) as a cryoprotectant at different levels (3%, 6%, or 9%) on the post-thawed sperm quality, motility, antioxidant-biomarkers, and the expression of anti-freeze related genes. Semen samples were collected twice a week from twelve roosters aged 40 wk, weighing 3400 ± 70 g, and belonging to the Cairo-B2 chicken strain. Fresh semen samples were rapidly appraised, pooled, diluted with two volumes of a basic extender, and divided equally into three groups. The diluted groups were chilled at −20 °C for 7 min, then gently supplemented with 3, 6, or 9% pre-cooled DMA and equilibrated at 5 °C for a further 10 min. Semen pellets were formed by pipetting drops 7 cm above liquid nitrogen (LN2), which were then kept inside cryovials in the LN2. Thawing was performed 2 months later by taking 3–4 pellets of the frozen semen into a glass tube and warming it in a water bath for 8 s at 60 °C. The results showed that 3% DMA increased the proportion of total motile sperm, progressivity, viability, and plasma membrane integrity (%) compared to the 6% and 9% DMA groups. The lipid peroxidation and antioxidant enzyme activity were improved in the 3% group. At the same time, some anti-freeze-related genes’ (including ras homolog family member A (RHOA), heat shock protein 70 (HSP70), and small nuclear ribonucleoprotein polypeptide A (SNRPA1)) expressions were upregulated within the 3% DMA group relative to other groups. In conclusion, the 3% DMA group maintained higher post-thawed sperm quality than the other tested groups.
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